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Updated: Apr 30, 2026

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DYRK1A phoshorylates histone H3 to differentially regulate the binding of HP1 isoforms and antagonize HP1-mediated

Suk Min Jang1, Saliha Azebi1, Guillaume Soubigou2

  • 1Institut Pasteur, Dpt Biologie du Développement et Cellules Souches Unité de Régulation Epigénétique, Paris, France URA2578, CNRS, Paris, France Sorbonne Universités UPMC Univ Paris06, IFD, Paris cedex05, France.

EMBO Reports
|May 14, 2014
PubMed

Heterochromatin protein 1 (HP1) proteins are chromatin-bound transcriptional regulators. While their chromodomain binds histone H3 methylated on lysine 9, their chromoshadow domain associates with the H3 histone fold in a region involved in chromatin remodeling. Here, we show that phosphorylation at histone H3 threonine 45 and serine 57 within this latter region differentially affects binding of the three mammalian HP1 isoforms HP1α, HP1β and HP1γ. Both phosphorylation events are dependent on the activity of the DYRK1A kinase that antagonizes HP1-mediated transcriptional repression and participates in abnormal activation of cytokine genes in Down's syndrome-associated megakaryoblastic leukemia.

Keywords:
chromatin silencingcytokineepigenetichistone codeinflammation

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